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cell surface immunoglobulin 160 cellular and humoral metal hypersensitivity<br />

specific for surface antigens on lymphocyte subsets.<br />

Immunotoxicity procedures can be used to induce selective<br />

cytolysis of cells expressing a certain antigen at the cell<br />

surface by reacting the cell with antibodies. Immunoadhesion<br />

procedures make use of antibodies against cell-surface<br />

antigens bound to a solid support, permitting the capture of<br />

cells by adherence to the support. Immunomagnetic beads<br />

to which antibodies have been attached may also be used.<br />

Magnetic cell sorting is based on the use of monoclonal<br />

antibodies or lectins that bind specifically to surface antigen/<br />

receptor expressed by a certain cell subset. Flow cytometry<br />

is a precise and objective method to quantify the number<br />

of cells expressing a given surface marker and the extent to<br />

which the marker is expressed.<br />

cell surface immunoglobulin<br />

The B cell receptor for antigen.<br />

cell surface molecule immunoprecipitation<br />

A technique to analyze cell surface molecules with monoclonal<br />

antibodies and antisera. Immunoprecipitation is based on<br />

solubilization of membrane proteins by the use of nonionic<br />

detergents, subsequent interaction of specific antibody with<br />

solubilized membrane antigen, and recovery of antibody–<br />

antigen complexes by binding to an insoluble support that<br />

permits washing procedures to remove unbound molecules.<br />

Analysis of immunoprecipitates can be accomplished by<br />

sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis<br />

(SDS-PAGE) or isoelectric focusing (IEF).<br />

cell surface receptors and ligands<br />

Activation of caspases via ligand binding to cell surface<br />

receptors involves the tumor necrosis factor (TNF) family<br />

of receptors and ligands. These receptors contain an<br />

80-amino acid death domain (DD) that, through homophilic<br />

interactions, recruits adaptor proteins to form a signaling<br />

complex on the cytosolic surface of the receptor. The signaling<br />

induced by the ligand binding to the receptor appears<br />

to involve trimerization. Based on x-ray crystallography,<br />

the trimeric ligand has three equal faces, and a receptor<br />

monomer interacts at each of the three junctions formed by<br />

the three faces. Thus, each receptor polypeptide contacts<br />

TRAY<br />

POS<br />

1A<br />

1B<br />

1C<br />

1D<br />

1E<br />

1F<br />

2F<br />

2E<br />

2D<br />

2C<br />

2B<br />

2A<br />

3A<br />

3B<br />

3C<br />

3D<br />

3E<br />

3F<br />

4F<br />

4E<br />

#CENTRL<br />

TEST<br />

8<br />

8<br />

8<br />

8<br />

8<br />

8<br />

8<br />

8<br />

1<br />

1<br />

8<br />

1<br />

1<br />

1<br />

1<br />

1<br />

1<br />

1<br />

1<br />

1<br />

10571T<br />

9891T<br />

9884T<br />

9898T<br />

10356T<br />

10990T<br />

10367T<br />

7109T<br />

6606T<br />

10567T<br />

10988T<br />

10359T<br />

10549T<br />

10361T<br />

10570T<br />

9899T<br />

10352T<br />

10547T<br />

6688T<br />

10568T<br />

two ligands. The bringing together of three receptors,<br />

thereby orienting the intracellular DDs, appears to be the<br />

critical feature for signaling by these receptors. The adaptor<br />

proteins recruited to the aligned receptor DDs recruit either<br />

caspases or other signaling protiens. The exact mechanism<br />

by which recruitment of caspase 8 to the DD-induced complex<br />

causes activation of caspase 8 is not clear.<br />

cell tray panel<br />

Used to detect and identify human leukocyte antigen (HLA)<br />

antibodies. Patient serum is tested against a panel of known<br />

cells. The panel (or percent) reactive antibody (PRA) is the<br />

percent of panel cells reacting with a patient’s serum. It is<br />

expressed as a percentage of the total reactivity: % PRA =<br />

(number of positive reactions/ number of cells in panel) ×<br />

100. This percentage is a useful indicator of the proportion<br />

of HLA antibodies.<br />

cellular allergy<br />

Refer to delayed-type hypersensitivity, type IV cell-mediated<br />

hypersensitivity, and cell-mediated immunity.<br />

cellular and humoral metal hypersensitivity<br />

Metal ions interact with proteins in several ways. Mercury<br />

and gold form metal–protein complexes by binding with<br />

high affinity to thiol groups of cysteine. These complexes<br />

are able to activate T lymphocytes with or without antigen<br />

or by superantigen stimulation. Mercury is used as a preservative<br />

and as a dental amalgam, but mercury compounds<br />

can induce contact sensitivity and glomerulonephritis in<br />

humans. Gold salts are used as antirheumatic drugs but can<br />

cause contact dermatitis, stomatitis, pneumonitis, glomerulonephritis,<br />

increased levels of serum immunoglobulins,<br />

antinuclear autoantibodies, thrombocytopenia, and asthma<br />

in goldminers. Cadmium chloride can induce renal tubular<br />

damage in mice via interaction with T cells with specific<br />

Hsp70 on tubular cells. Occupational exposure to beryllium<br />

salts may lead to chronic interstitial granulomatous lung<br />

disease. CD4 + T lymphocytes from patients with berylliosis<br />

react to beryllium salts in a major histocompatibility<br />

complex (MHC) class II restricted manner. Silica, silicone,<br />

and sodium silicate activate CD4 + memory T lymphocytes<br />

CELL PANEL TYPING<br />

ID<br />

A B C BW<br />

6<br />

RACE<br />

H<br />

C<br />

B<br />

B<br />

B<br />

O<br />

C<br />

H<br />

C<br />

C<br />

C<br />

C<br />

O<br />

O<br />

O<br />

B<br />

O<br />

C<br />

C<br />

H<br />

Cell tray panel showing positive reactions (8s) for HLA-A1 at tray positions 1A, 1B, 1C, 1D, 1E, lF, 2F, and 2E and a positive reaction for HLA-A24 at<br />

position 2B.<br />

1<br />

1<br />

1<br />

1<br />

1<br />

1<br />

1<br />

1<br />

2<br />

2<br />

2<br />

2<br />

2<br />

2<br />

2<br />

2<br />

2<br />

2<br />

2<br />

2<br />

2<br />

2<br />

2<br />

23<br />

23<br />

24<br />

32<br />

11<br />

11<br />

24<br />

25<br />

26<br />

26<br />

26<br />

30<br />

30<br />

31<br />

31<br />

32<br />

8<br />

44<br />

57<br />

45<br />

58<br />

27<br />

8<br />

13<br />

18<br />

37<br />

51<br />

57<br />

39<br />

54<br />

60<br />

8<br />

13<br />

35<br />

50<br />

41<br />

35<br />

51<br />

82<br />

49<br />

72<br />

37<br />

51<br />

64<br />

38<br />

60<br />

55<br />

62<br />

61<br />

62<br />

65<br />

58<br />

46<br />

47<br />

60<br />

61<br />

7<br />

1<br />

3<br />

6<br />

6<br />

2<br />

7<br />

6<br />

7<br />

3<br />

3<br />

5<br />

1<br />

1<br />

4<br />

7<br />

1<br />

4<br />

3<br />

2<br />

5<br />

6<br />

7<br />

6<br />

8<br />

6<br />

6<br />

7<br />

3<br />

8<br />

6<br />

6<br />

7<br />

4<br />

4<br />

4<br />

4<br />

4<br />

4<br />

4<br />

4<br />

4<br />

4<br />

4<br />

4<br />

4<br />

4<br />

6<br />

6<br />

6<br />

6<br />

6<br />

6<br />

6<br />

6<br />

6<br />

6<br />

6<br />

6<br />

6<br />

6<br />

6<br />

6<br />

6

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